ID U5BS93_9BACT Unreviewed; 1051 AA.
AC U5BS93;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=P872_20970 {ECO:0000313|EMBL:ERM80778.1};
OS Rhodonellum psychrophilum GCM71 = DSM 17998.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Rhodonellum.
OX NCBI_TaxID=1123057 {ECO:0000313|EMBL:ERM80778.1, ECO:0000313|Proteomes:UP000016843};
RN [1] {ECO:0000313|EMBL:ERM80778.1, ECO:0000313|Proteomes:UP000016843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GCM71 {ECO:0000313|EMBL:ERM80778.1,
RC ECO:0000313|Proteomes:UP000016843};
RX PubMed=24309741;
RA Hauptmann A.L., Glaring M.A., Hallin P.F., Prieme A., Stougaard P.;
RT "Draft Genome Sequence of the Psychrophilic and Alkaliphilic Rhodonellum
RT psychrophilum Strain GCM71T.";
RL Genome Announc. 1:e01014-13(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERM80778.1}.
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DR EMBL; AWXR01000077; ERM80778.1; -; Genomic_DNA.
DR RefSeq; WP_019599403.1; NZ_KB906686.1.
DR AlphaFoldDB; U5BS93; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG1807; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR Proteomes; UP000016843; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR031621; HisKA_7TM.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF16927; HisKA_7TM; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000016843};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 38..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 561..784
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 815..933
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 955..1051
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 866
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 994
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1051 AA; 118955 MW; 5F4E0838BC218DC1 CRC64;
MAELSFNLFS IPIFFTSLLF LVLIFLSYDK ENRSGEVYFC LLLFSCFVYS FLYGMELIST
SEEAIVHFFQ LEFFGGVFLT PLLLAFVVKY TGNSRYFKPK IWVLIFGIPV FFLIMSQTNA
YHHLFFIELS TKQNAYFNAI SFTPGILYWV YAIFNVVPVL FANYLLFRML SRVPKIFSVQ
VTILLIGTLI PWSFHIVDLL GYSPYSMDLV PFSLGISSVI IYLGLFKYGL FKNAPVAFKT
IFENLLDGVL ILNNKGEIIT QNQAAIQFFQ KSTIYNLLTK KELLQNWPQL TPLFNLENFS
EQVELHHPEE NRVLSAYREN RRNQKGWDND FHYIIIKDIT VQKSAEATIR SKELALQTIN
TSLLRNEKML KSIAMATKEL LSNTKFNKAA QKAISILGDG AGVDRAYLFE NTIHENGKIT
SSQRFEWSAS AVAPEIDNPG LQYLPLELFG EAVDFISSNK IYQAIVSKIS TDPELKELLE
SQEIKSILLI PIFVKEDFWG FVGFDDCVTE RIWSEAEAAL LISFADSISN AIERKTLELN
LFKSMQQAKE ASIAKSEFLA NMSHEIRTPL NGVIGFSDLL MRTGLNETQK EYLKSIFQSG
NLLLDLINDI LDFSKIEAGK LALNPIKVNL KKMTQEALTV VQPLAEEKGL KLLLLQDLKT
PKFSFLDDIR VKQILINLLS NAIKFTATGH VELAIKVKSI RLEEKLALVE FSVTDTGIGI
SKEKEKVIFE AFAQEDNSTT RKYGGTGLGL TISNKLLALM DSRLELETTF GKGSKFSFLL
TLPYEEGEVS SEDFSNKTIE SPPRPVTNNI KKGFKFLLVD DNPVNMLLAK TIVKNIVPSA
ILLEAKNGKL AVDLFAQNKP DMVFMDIQMP EMSGYEATEN IRKLETSSRT PIIALTAGTV
LGEYERCLEA GMDDYLSKPI VVSDISNMIQ KYLGTTSPKE ALHFLAKFDE FKTNDPAFFQ
ELIQMSKTNL EKLNSELMHF WIEKNLNLVK QTGHSLKGLA LNMDFEHLVK LASNVEKLQD
LAGDETESLM FQIGSEIKQI IKSLELELIN I
//
